Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-11-21
pubmed:abstractText
A fluorescent probe has been employed to study the status of a tumour associated protease, guanidinobenzoatase, in frozen sections of human tumours obtained from the head and neck regions. The results indicate that in vivo a naturally occurring inhibitor of guanidinobenzoatase effectively controls the activity of this enzyme on the majority of cells in a tumour mass. This inhibitor can be artificially displaced by formaldehyde treatment of the frozen sections and this treatment reveals the extent of latent enzyme in the section. In the frozen sections it was noticed that at the advancing edges of the tumour mass, the tumour cells possessed uninhibited guanidinobenzoatase, an enzyme known to degrade the link peptide between cells and fibronectin. It was shown that a synthetic inhibitor of guanidinobenzoatase selectively inhibited the guanidinobenzoatase of the tumour cells at the advancing edge of the tumour mass. It is suggested that the guanidinobenzoatase on cells at the leading edge of the tumour mass plays an important role in the invasion of adjacent host tissue. This synthetic inhibitor of guanidinobenzoatase has no inhibitory action on other trypsin-like enzymes and might therefore be of value in limiting the growth of the tumour mass in vivo.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0007-0920
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-60
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Studies on the activity of a protease associated with cells at the advancing edge of human tumour masses in frozen sections.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't